Three kinds of extracellular glucosyltransferases from Streptococcus mutans 6715 (serotype g) |
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Authors: | A Shimamura H Tsumori H Mukasa |
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Institution: | Department of Chemistry, National Defense Medical College, 2, Namiki 3-chome, Tokorozawa, Saitama 359, Japan |
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Abstract: | In addition to the 1,3-alpha-D-glucan synthetase (pI 4.9) and the highly-branched 1,6-alpha-D-glucan synthetase (pI 3.9-4.1), Streptococcus mutans 6715 (serotype g) was found to secrete the third glucosyltransferase in multiple forms (pI 5.5-7.0), which exhibited 87% 1,6-alpha-bond-, 6% 1,3-alpha-bond- and 7% 1,3,6-branch-forming activities. The production of this enzyme was extremely enhanced when the organism was grown in Tween 80-supplemented medium. The 3 glucosyltransferases from the same organism were enzymatically and immunologically distinct from each other, and they were commonly found among the serotype g strains. |
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Keywords: | Glucosyltransferase Glucan Tween 80 IEF isoelectric focusing PAS periodic acid-Schiff base |
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